Resolution of Holliday junctions by eukaryotic DNA topoisomerase I Journal Article

   


Authors: Sekiguchi, J.; Seeman, N. C.; Shuman, S.
Article Title: Resolution of Holliday junctions by eukaryotic DNA topoisomerase I
Abstract: The Holliday junction, a key intermediate in both homologous and site- specific recombination, is generated by the reciprocal exchange of single strands between two DNA duplexes. Resolution of the junctions can occur in two directions with respect to flanking markers, either restoring the parental DNA configuration or generating a genetic crossover. Recombination can he regulated, in principle, by factors that influence the directionality of the resolution step. We demonstrate that the vaccinia virus DNA topoisomerase, a eukaryotic type I enzyme, catalyzes resolution of synthetic Holliday junctions in vitro. The mechanism entails concerted transesterifications at two recognition sites, 5'-CCCTT↓, that are opposed within a partially mobile four-way junction. Cruciforms are resolved unidirectionally and with high efficiency into two linear duplexes. These findings suggest a model whereby type I topoisomerases may either promote or suppress genetic recombination in vivo.
Keywords: nonhuman; enzyme activity; dna; double stranded dna; genetic recombination; molecular sequence data; recombination, genetic; vaccinia virus; base sequence; nucleic acid conformation; sequence homology; dna topoisomerase; dna topoisomerases, type i; dna nucleotidyltransferases; transposases; eukaryotic cells; holliday junction; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 93
Issue: 2
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1996-01-23
Start Page: 785
End Page: 789
Language: English
DOI: 10.1073/pnas.93.2.785
PUBMED: 8570635
PROVIDER: scopus
PMCID: PMC40133
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030061445&doi=10.1073%2fpnas.93.2.785&partnerID=40&md5=bf9f099b4fce576d5f65dd1e02d01726
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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MSK Authors
  1. Stewart H Shuman
    546 Shuman
  2. JoAnn M. Sekiguchi
    18 Sekiguchi
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